+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 8j8z | |||||||||||||||
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タイトル | Structure of beta-arrestin1 in complex with D6Rpp | |||||||||||||||
要素 |
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キーワード | SYGNALING PROTEIN/IMMUNE SYSTEM / GPCR / Arrestin / SIGNALING PROTEIN / SYGNALING PROTEIN-IMMUNE SYSTEM complex | |||||||||||||||
機能・相同性 | 機能・相同性情報 V2 vasopressin receptor binding / alpha-1A adrenergic receptor binding / follicle-stimulating hormone receptor binding / TGFBR3 regulates TGF-beta signaling / sensory perception of touch / G alpha (s) signalling events / alpha-1B adrenergic receptor binding / follicle-stimulating hormone signaling pathway / protein phosphorylated amino acid binding / angiotensin receptor binding ...V2 vasopressin receptor binding / alpha-1A adrenergic receptor binding / follicle-stimulating hormone receptor binding / TGFBR3 regulates TGF-beta signaling / sensory perception of touch / G alpha (s) signalling events / alpha-1B adrenergic receptor binding / follicle-stimulating hormone signaling pathway / protein phosphorylated amino acid binding / angiotensin receptor binding / Lysosome Vesicle Biogenesis / AP-2 adaptor complex binding / Golgi Associated Vesicle Biogenesis / chemokine receptor activity / MAP2K and MAPK activation / Ub-specific processing proteases / positive regulation of smooth muscle cell apoptotic process / negative regulation of interleukin-8 production / Cargo recognition for clathrin-mediated endocytosis / C-C chemokine receptor activity / Clathrin-mediated endocytosis / clathrin adaptor activity / scavenger receptor activity / C-C chemokine binding / regulation of G protein-coupled receptor signaling pathway / arrestin family protein binding / G protein-coupled receptor internalization / Chemokine receptors bind chemokines / Thrombin signalling through proteinase activated receptors (PARs) / response to morphine / mitogen-activated protein kinase kinase binding / positive regulation of Rho protein signal transduction / clathrin binding / stress fiber assembly / negative regulation of Notch signaling pathway / positive regulation of receptor internalization / pseudopodium / positive regulation of insulin secretion involved in cellular response to glucose stimulus / negative regulation of interleukin-6 production / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / phototransduction / clathrin-coated pit / negative regulation of protein ubiquitination / insulin-like growth factor receptor binding / visual perception / GTPase activator activity / negative regulation of protein phosphorylation / cell chemotaxis / positive regulation of protein ubiquitination / actin filament / nuclear estrogen receptor binding / G protein-coupled receptor binding / phosphoprotein binding / calcium-mediated signaling / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / recycling endosome / negative regulation of ERK1 and ERK2 cascade / endocytosis / protein transport / positive regulation of peptidyl-serine phosphorylation / positive regulation of cytosolic calcium ion concentration / ubiquitin-dependent protein catabolic process / cytoplasmic vesicle / basolateral plasma membrane / nuclear membrane / regulation of apoptotic process / postsynaptic membrane / proteasome-mediated ubiquitin-dependent protein catabolic process / negative regulation of neuron apoptotic process / transmembrane transporter binding / positive regulation of MAPK cascade / dendritic spine / transcription coactivator activity / positive regulation of ERK1 and ERK2 cascade / postsynaptic density / early endosome / intracellular signal transduction / endosome / protein ubiquitination / inflammatory response / immune response / response to xenobiotic stimulus / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / external side of plasma membrane / intracellular membrane-bounded organelle / signaling receptor binding / glutamatergic synapse / positive regulation of cell population proliferation / ubiquitin protein ligase binding / regulation of DNA-templated transcription / chromatin / negative regulation of apoptotic process / regulation of transcription by RNA polymerase II / enzyme binding / positive regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / plasma membrane / cytosol 類似検索 - 分子機能 | |||||||||||||||
生物種 | Rattus norvegicus (ドブネズミ) Mus musculus (ハツカネズミ) Homo sapiens (ヒト) | |||||||||||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.4 Å | |||||||||||||||
データ登録者 | Maharana, J. / Sarma, P. / Yadav, M.K. / Chami, M. / Banerjee, R. / Shukla, A.K. | |||||||||||||||
資金援助 | インド, 4件
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引用 | ジャーナル: Science / 年: 2024 タイトル: Molecular insights into atypical modes of β-arrestin interaction with seven transmembrane receptors. 著者: Jagannath Maharana / Fumiya K Sano / Parishmita Sarma / Manish K Yadav / Longhan Duan / Tomasz M Stepniewski / Madhu Chaturvedi / Ashutosh Ranjan / Vinay Singh / Sayantan Saha / Gargi Mahajan ...著者: Jagannath Maharana / Fumiya K Sano / Parishmita Sarma / Manish K Yadav / Longhan Duan / Tomasz M Stepniewski / Madhu Chaturvedi / Ashutosh Ranjan / Vinay Singh / Sayantan Saha / Gargi Mahajan / Mohamed Chami / Wataru Shihoya / Jana Selent / Ka Young Chung / Ramanuj Banerjee / Osamu Nureki / Arun K Shukla / 要旨: β-arrestins (βarrs) are multifunctional proteins involved in signaling and regulation of seven transmembrane receptors (7TMRs), and their interaction is driven primarily by agonist-induced receptor ...β-arrestins (βarrs) are multifunctional proteins involved in signaling and regulation of seven transmembrane receptors (7TMRs), and their interaction is driven primarily by agonist-induced receptor activation and phosphorylation. Here, we present seven cryo-electron microscopy structures of βarrs either in the basal state, activated by the muscarinic receptor subtype 2 (M2R) through its third intracellular loop, or activated by the βarr-biased decoy D6 receptor (D6R). Combined with biochemical, cellular, and biophysical experiments, these structural snapshots allow the visualization of atypical engagement of βarrs with 7TMRs and also reveal a structural transition in the carboxyl terminus of βarr2 from a β strand to an α helix upon activation by D6R. Our study provides previously unanticipated molecular insights into the structural and functional diversity encoded in 7TMR-βarr complexes with direct implications for exploring novel therapeutic avenues. | |||||||||||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 8j8z.cif.gz | 240.8 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb8j8z.ent.gz | 182.9 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 8j8z.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
文書・要旨 | 8j8z_validation.pdf.gz | 1.1 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 8j8z_full_validation.pdf.gz | 1.1 MB | 表示 | |
XML形式データ | 8j8z_validation.xml.gz | 46.1 KB | 表示 | |
CIF形式データ | 8j8z_validation.cif.gz | 69.3 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/j8/8j8z ftp://data.pdbj.org/pub/pdb/validation_reports/j8/8j8z | HTTPS FTP |
-関連構造データ
関連構造データ | 36082MC 8go9C 8j8rC 8j8vC 8j97C 8j9kC 8ja3C 8jafC M: このデータのモデリングに利用したマップデータ C: 同じ文献を引用 (文献) |
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類似構造データ | 類似検索 - 機能・相同性F&H 検索 |
-リンク
-集合体
登録構造単位 |
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1 |
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-要素
#1: タンパク質 | 分子量: 47088.508 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Rattus norvegicus (ドブネズミ) / 遺伝子: Arrb1 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: P29066 #2: 抗体 | 分子量: 25512.354 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Mus musculus (ハツカネズミ) / 発現宿主: Escherichia coli (大腸菌) #3: 抗体 | 分子量: 23435.064 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Mus musculus (ハツカネズミ) / 発現宿主: Escherichia coli (大腸菌) #4: タンパク質・ペプチド | 分子量: 2352.668 Da / 分子数: 2 / Fragment: C-terminal tail / 由来タイプ: 合成 / 由来: (合成) Homo sapiens (ヒト) / 参照: UniProt: O00590 研究の焦点であるリガンドがあるか | Y | Has protein modification | Y | |
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-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
-試料調製
構成要素 |
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分子量 |
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由来(天然) |
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由来(組換発現) |
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緩衝液 | pH: 7.4 | ||||||||||||||||||||||||||||||||||||
緩衝液成分 |
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試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | ||||||||||||||||||||||||||||||||||||
急速凍結 | 凍結剤: ETHANE |
-電子顕微鏡撮影
顕微鏡 | モデル: TFS GLACIOS |
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電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 200 kV / 照射モード: FLOOD BEAM |
電子レンズ | モード: BRIGHT FIELD / 倍率(公称値): 46000 X / 最大 デフォーカス(公称値): 2500 nm / 最小 デフォーカス(公称値): 500 nm / Cs: 2.7 mm |
試料ホルダ | 凍結剤: NITROGEN |
撮影 | 電子線照射量: 53 e/Å2 / 検出モード: COUNTING / フィルム・検出器のモデル: GATAN K3 (6k x 4k) / 実像数: 9698 |
画像スキャン | 動画フレーム数/画像: 40 |
-解析
ソフトウェア | 名称: PHENIX / バージョン: 1.20.1_4487: / 分類: 精密化 | ||||||||||||||||||||||||||||
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EMソフトウェア |
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CTF補正 | タイプ: NONE | ||||||||||||||||||||||||||||
粒子像の選択 | 選択した粒子像数: 5300908 | ||||||||||||||||||||||||||||
3次元再構成 | 解像度: 3.4 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 369871 / 対称性のタイプ: POINT | ||||||||||||||||||||||||||||
原子モデル構築 | プロトコル: FLEXIBLE FIT / 空間: REAL | ||||||||||||||||||||||||||||
原子モデル構築 | PDB-ID: 8GO8 Accession code: 8GO8 / Source name: PDB / タイプ: experimental model | ||||||||||||||||||||||||||||
拘束条件 |
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